issue contents

ISSN: 2053-230X

September 2020 issue

Highlighted illustration

Cover illustration: The structure of the Moco carrier protein from Rippkaea orientalis [Krausze et al. (2020), Acta Cryst. F76, 453-463]. The molybdenum cofactor (Moco) is the prosthetic group of all molybdenum-dependent enzymes except for nitrogenase, but the mechanisms of Moco transfer, storage and insertion are not well understood. Here the search for potential Moco carrier proteins has been extended to the prokaryotes with the study of a putative MCP from R. orientalis.


research communications

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A case of contamination from a Serratia bacterial strain that occurred while attempting to crystallize an unrelated protein from Burkholderia pseudomallei (overexpressed in E. coli) is presented. The procedures that were adopted to identify the contaminant based on crystallographic data only are presented and the crystal structure of Serrata spp. cyanate hydratase is briefly discussed.

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A structure is reported of the E. coli transcription terminator factor Rho that was crystallized as an impurity present in preparations of an overexpressed bacterial membrane-transport protein.

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The crystal structure of full-length glyceraldehyde-3-phosphate dehydrogenase type 1 (GAPDH1) from Escherichia coli was determined at 1.88 Å resolution. Analysis of the NAD+-bound form showed some differences between the structures of E. coli GAPDH1 and human GAPDH. As E. coli GAPDH1 shares 100% identity with GAPDH from Shigella sonnei, its structure may help in finding a drug for the treatment of shigellosis.

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The structure of PfGH50B reveals a two-domain structure consisting of a β-sandwich CBM-like domain fused to an (α/β)8-barrel catalytic domain. Key structural features that are likely to influence the nature of the reaction products and the enzyme processivity are revealed by structural comparisons.

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Histone deacetylase 6 (HDAC6) is an emerging target for the treatment of various diseases such as cancer through selective inhibition. While the second catalytic domain (HDAC6 CD2) has been extensively studied, comparatively little research has focused on the first catalytic domain (HDAC6 CD1). This work provides new structural insights regarding inhibitor binding to HDAC6 CD1 enabled by the study of active-site mutants.

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SbtB was crystallized in a new crystal form and was found to adopt a tetrameric conformation in the crystal rather than the native trimeric conformation. Cys94 was found to form intermolecular disulfide bonds between adjacent SbtB molecules in the crystal lattice.

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The structure of native cytochrome c6 isolated from T. elongatus was solved by X-ray crystallography and two different space groups were identified. The high-resolution structures and complementary biophysical characterization in solution indicate interaction interfaces that could enable distinct functionality in photosynthesis. In addition, a post-translational methylation is indicated.

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The structure of a Moco carrier protein from Rippkaea orientalis is presented together with evidence for its selective binding of the mononucleotide variety of molybdenum cofactor.
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